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Structural evolution of the membrane-coating module of the nuclear pore complex.

Liu X, Mitchell JM, Wozniak RW, Blobel G, Fan J
Proc Natl Acad Sci U S A 109 16498-503 (2012)
Cited: 17 times
EuropePMC logo PMID: 23019579

Abstract

The coatomer module of the nuclear pore complex borders the cylinder-like nuclear pore-membrane domain of the nuclear envelope. In evolution, a single coatomer module increases in size from hetero-heptamer (Saccharomyces cerevisiae) to hetero-octamer (Schizosaccharomyces pombe) to hetero-nonamer (Metazoa). Notably, the heptamer-octamer transition proceeds through the acquisition of the nucleoporin Nup37. How Nup37 contacts the heptamer remained unknown. Using recombinant nucleoporins, we show that Sp-Nup37 specifically binds the Sp-Nup120 member of the hetero-heptamer but does not bind an Sc-Nup120 homolog. To elucidate the Nup37-Nup120 interaction at the atomic level, we carried out crystallographic analyses of Sp-Nup37 alone and in a complex with an N-terminal, ~110-kDa fragment of Sp-Nup120 comprising residues 1-950. Corroborating structural predictions, we determined that Nup37 folds into a seven-bladed β-propeller. Several disordered surface regions of the Nup37 β-propeller assume structure when bound to Sp-Nup120. The N-terminal domain of Sp-Nup120(1-950) also folds into a seven-bladed propeller with a markedly protruding 6D-7A insert and is followed by a contorted helical domain. Conspicuously, this 6D-7A insert contains an extension of 50 residues which also is highly conserved in Metazoa but is absent in Sc-Nup120. Strikingly, numerous contacts with the Nup37 β-propeller are located on this extension of the 6D-7A insert. Another contact region is situated toward the end of the helical region of Sp-Nup120(1-950). Our findings provide information about the evolution and the assembly of the coatomer module of the nuclear pore complex.

Articles - 4gq2 mentioned but not cited (3)

  1. In situ structural analysis of the human nuclear pore complex. von Appen A, Kosinski J, Sparks L, Ori A, DiGuilio AL, Vollmer B, Mackmull MT, Banterle N, Parca L, Kastritis P, Buczak K, Mosalaganti S, Hagen W, Andres-Pons A, Lemke EA, Bork P, Antonin W, Glavy JS, Bui KH, Beck M. Nature 526 140-143 (2015)
  2. Structural evolution of the membrane-coating module of the nuclear pore complex. Liu X, Mitchell JM, Wozniak RW, Blobel G, Fan J. Proc Natl Acad Sci U S A 109 16498-16503 (2012)
  3. WD40 domain of Apc1 is critical for the coactivator-induced allosteric transition that stimulates APC/C catalytic activity. Li Q, Chang L, Aibara S, Yang J, Zhang Z, Barford D. Proc Natl Acad Sci U S A 113 10547-10552 (2016)


Reviews citing this publication (4)

  1. The Nuclear Pore Complex as a Flexible and Dynamic Gate. Knockenhauer KE, Schwartz TU. Cell 164 1162-1171 (2016)
  2. The Structure of the Nuclear Pore Complex (An Update). Lin DH, Hoelz A. Annu Rev Biochem 88 725-783 (2019)
  3. The Structure Inventory of the Nuclear Pore Complex. Schwartz TU. J Mol Biol 428 1986-2000 (2016)
  4. Towards understanding nuclear pore complex architecture and dynamics in the age of integrative structural analysis. Hurt E, Beck M. Curr Opin Cell Biol 34 31-38 (2015)

Articles citing this publication (10)

  1. Integrated structural analysis of the human nuclear pore complex scaffold. Bui KH, von Appen A, DiGuilio AL, Ori A, Sparks L, Mackmull MT, Bock T, Hagen W, Andrés-Pons A, Glavy JS, Beck M. Cell 155 1233-1243 (2013)
  2. Atomic structure of the Y complex of the nuclear pore. Kelley K, Knockenhauer KE, Kabachinski G, Schwartz TU. Nat Struct Mol Biol 22 425-431 (2015)
  3. Ring cycle for dilating and constricting the nuclear pore. Solmaz SR, Blobel G, Melcák I. Proc Natl Acad Sci U S A 110 5858-5863 (2013)
  4. Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy. Thierbach K, von Appen A, Thoms M, Beck M, Flemming D, Hurt E. Structure 21 1672-1682 (2013)
  5. Characterization of nuclear pore complex components in fission yeast Schizosaccharomyces pombe. Asakawa H, Yang HJ, Yamamoto TG, Ohtsuki C, Chikashige Y, Sakata-Sogawa K, Tokunaga M, Iwamoto M, Hiraoka Y, Haraguchi T. Nucleus 5 149-162 (2014)
  6. Structure and nucleic acid binding activity of the nucleoporin Nup157. Seo HS, Blus BJ, Jankovic NZ, Blobel G. Proc Natl Acad Sci U S A 110 16450-16455 (2013)
  7. Functional genomics evidence unearths new moonlighting roles of outer ring coat nucleoporins. Katsani KR, Irimia M, Karapiperis C, Scouras ZG, Blencowe BJ, Promponas VJ, Ouzounis CA. Sci Rep 4 4655 (2014)
  8. Crystal structure of human nuclear pore complex component NUP43. Xu C, Li Z, He H, Wernimont A, Li Y, Loppnau P, Min J. FEBS Lett 589 3247-3253 (2015)
  9. Identification of AAAS gene mutation in Allgrove syndrome: A report of three cases. Li W, Gong C, Qi Z, Wu DI, Cao B. Exp Ther Med 10 1277-1282 (2015)
  10. Integration and deconvolution methodology deciphering prognosis-related signatures in lung adenocarcinoma. Yi M, Shi J, Tan X, Zhang X, Tao D, Yang Y, Liu Y. J Cancer Res Clin Oncol 149 16441-16460 (2023)


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